A retinoic acid receptor α antagonist counteracts retinoid teratogenicity in vitro and reduced incidence and/or severity of malformations in vivo

1994 ◽  
Vol 70 (3) ◽  
pp. 299-308 ◽  
Author(s):  
Karl Eckhardt ◽  
Georg Schmitt
Keyword(s):  
Retinoic Acid ◽  
Retinoic Acid Receptor ◽  
Acid Receptor ◽  
Teratogenicity In Vitro ◽  
Retinoic Acid Receptor Α

scholarly journals Pharmacological Activity of Retinoic Acid Receptor Alpha-Selective Antagonists in Vitro and in Vivo

2013 ◽  
Vol 4 (5) ◽  
pp. 446-450 ◽  
Author(s):  
Sanny S. W. Chung ◽  
Rebecca A. D. Cuellar ◽  
Xiangyuan Wang ◽  
Peter R. Reczek ◽  
Gunda I. Georg ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Pharmacological Activity ◽  
Retinoic Acid Receptor ◽  
Retinoic Acid Receptor Alpha ◽  
Acid Receptor ◽  
Receptor Alpha ◽  
Selective Antagonists

scholarly journals Ligand-Dependent Regulation of Retinoic Acid Receptor α in Rat Testis: In Vivo Response to Depletion and Repletion of Vitamin A

Endocrinology ◽  
1998 ◽  
Vol 139 (3) ◽  
pp. 1239-1248 ◽  
Author(s):  
Karin M. Akmal ◽  
Jannette M. Dufour ◽  
Mynuong Vo ◽  
Sarah Higginson ◽  
Kwan Hee Kim
Keyword(s):  
Retinoic Acid ◽  
Vitamin A ◽  
Retinoic Acid Receptor ◽  
Acid Receptor ◽  
Rat Testis ◽  
Retinoic Acid Receptor Α

scholarly journals Identification of Transcripts Initiated from an Internal Promoter in the c-erbAα Locus That Encode Inhibitors of Retinoic Acid Receptor-α and Triiodothyronine Receptor Activities

1997 ◽  
Vol 11 (9) ◽  
pp. 1278-1290 ◽  
Author(s):  
Olivier Chassande ◽  
Alexandre Fraichard ◽  
Karine Gauthier ◽  
Frédéric Flamant ◽  
Claude Legrand ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Transcriptional Activation ◽  
Hormone Receptors ◽  
Thyroid Hormone Receptor ◽  
Retinoic Acid Receptor ◽  
Expression Patterns ◽  
Internal Promoter ◽  
Acid Receptor ◽  
Retinoic Acid Receptor Α

Abstract The thyroid hormone receptor-coding locus, c-erbAα, generates several mRNAs originating from a single primary transcript that undergoes alternative splicing. We have identified for the first time two new transcripts, called TRΔα1 and TRΔα2[ mRNA for isoform α1 and α2 of the T3 receptor (TR), respectively], whose transcription is initiated from an internal promoter located within intron 7 of the c-erbAα gene. These two new transcripts exhibit tissue-specific patterns of expression in the mouse. These two patterns are in sharp contrast with the expression patterns of the full-length transcripts generated from the c-erbAα locus. TRΔα1 and TRΔα2 mRNAs encode N-terminally truncated isoforms of T3Rα1 and T3Rα2, respectively. The protein product of TRΔα1 antagonizes the transcriptional activation elicited by T3 and retinoic acid. This protein inhibits the ligand-induced activating functions of T3Rα1 and 9-cis-retinoic acid receptor-α but does not affect the retinoic acid-dependent activating function of retinoic acid receptor-α. We predict that these truncated proteins may work as down-regulators of transcriptional activity of nuclear hormone receptors in vivo.

In vitro binding of retinoids to the nuclear retinoic acid receptor α

1990 ◽  
Vol 186 (1) ◽  
pp. 19-23 ◽  
Author(s):  
M.T. Cavey ◽  
B. Martin ◽  
I. Carlavan ◽  
B. Shroot
Keyword(s):  
Retinoic Acid ◽  
Retinoic Acid Receptor ◽  
Acid Receptor ◽  
In Vitro Binding ◽  
Vitro Binding ◽  
Retinoic Acid Receptor Α

Retinoic Acid Inhibits Nitric Oxide Synthase-2 Expression through the Retinoic Acid Receptor-α

2000 ◽  
Vol 270 (3) ◽  
pp. 846-851 ◽  
Author(s):  
Allan Sirsjö ◽  
Andreas C Gidlöf ◽  
Anneli Olsson ◽  
Hans Törmä ◽  
Mikko Ares ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Retinoic Acid ◽  
Nitric Oxide Synthase ◽  
Retinoic Acid Receptor ◽  
Acid Receptor ◽  
Retinoic Acid Receptor Α ◽  
Nitric Oxide Synthase 2 ◽  
Oxide Synthase
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